Open AccessHelix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. 11. Lysine Parameters from Random Poly(hydroxybutylglutamine-co-L-lysine)
Author(s) -
M. K. Dygert,
G. T. Taylor,
F. Cardinaux,
Harold A. Scheraga
Publication year - 1976
Publication title -
macromolecules (print)
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.994
H-Index - 313
eISSN - 1520-5835
pISSN - 0024-9297
DOI - 10.1021/ma60053a021
Subject(s) - lysine , chemistry , random coil , helix (gastropod) , amino acid , stereochemistry , crystallography , circular dichroism , biochemistry , biology , ecology , snail
The synthesis and characterization of water-soluble random copolymers containing L-lysine with N5-(4-hydroxybutyl)-L-glutamine, and the thermally induced helix-coil transitions of these copolymers in water, are described. The incorporation of L-lysine was found to decrease the helix content of the polymers at neutral pH. The Zimm-Bragg parameters sigma and s for the helix-coil transition in poly(L-lysine) in water were deduced from an analysis of the melting curves in the manner described in earlier papers. The computed values of s indicate that, in the temperature range of 0-60 degrees C, lysine has a tendency to destabilize helical sequences, this tendency being minimal at approximately 25 degrees C and increasing at lower and higher temperatures.